| Primary Identifier | IPR030385 | Type | Domain |
| Short Name | G_IRG_dom |
| description | The P-loop guanosine triphosphatases (GTPases) control amultitude of biological processes, ranging from cell division, cell cycling,and signal transduction, to ribosome assembly and protein synthesis. GTPasesexert their control by interchanging between an inactive GDP-bound state andan active GTP-bound state, thereby acting as molecular switches. The commondenominator of GTPases is the highly conserved guanine nucleotide-binding (G)domain that is responsible for binding and hydrolysis of guanine nucleotides.The p47 or immunity-related GTPases (IRG) are at least as old as thevertebrates. The IRG proteins are an essential resistance system in the mousefor immunity against pathogens that enter the cell via a vacuole. Despite itsimportance for the mouse, the IRG resistance system is absent from humansbecause it has been lost during the divergent evolution of the primates. TheIRG proteins appear to be accompanied phylogenetically by homologous proteins,named 'quasi IRG' (IRGQ) proteins, that probably lack nucleotide binding orhydrolysis function, and that may form regulatory heterodimers with functionalIRG proteins. The region of lowest similarity is in the G domain, andconserved GTP-binding motifs are lacking [, , ]. |
